Accessibility of epsilon-amino groups of lysine to guanidination in kappa-elastin from bovine ligamentum nuchae.
Kappa-Elastin contains 3.81 lysyl residues per 1000 residues of amino acids. Among these residues, free epsilon-amino groups represent about 16 p. 100, as revealed by guanidination, the buried lysyl residues (buried epsilon-amino groups) represent about 33 p. 100, as revealed by dansylation. After drastic reduction by borohydride, no aldimine bonds were detected and only 6 p. 100 of "deeply buried" amino groups of lysyl residues were detected by a second dansylation. The remaining lysines (about 46 p. 100) are engaged or inaccessible.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004549:Elastin / Q000378:metabolism*; D006147:Guanine / Q000378:metabolism; D008022:Ligaments / Q000378:metabolism; D008239:Lysine / Q000378:metabolism*
D006147:Guanine; D004549:Elastin; D008239:Lysine